5L17

The crystal structure of neuraminidase in complex with zanamivir from A/Shanghai/2/2013 (H7N9) influenza virus

Summary for 5L17

• Entry DOI: 10.2210/pdb5l17/pdb
• Related: 5L14 5L15 5L18
• Descriptor: Neuraminidase, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: neuraminidase, h7n9, hydrolase
• Biological source: Influenza A virus
• Cellular location: Host apical cell membrane ; Single-pass type II membrane protein : R4NFR6
• Total number of polymer chains: 1
• Total formula weight: 46408.14

Authors

Yang, H.,Stevens, J. (deposition date: 2016-07-28, release date: 2017-08-09, Last modification date: 2024-11-06)

Primary citation

Gubareva, L.V.,Sleeman, K.,Guo, Z.,Yang, H.,Hodges, E.,Davis, C.T.,Baranovich, T.,Stevens, J.
Drug Susceptibility Evaluation of an Influenza A(H7N9) Virus by Analyzing Recombinant Neuraminidase Proteins.
J. Infect. Dis., 216:S566-S574, 2017

PubMed Abstract: Neuraminidase (NA) inhibitors are the recommended antiviral medications for influenza treatment. However, their therapeutic efficacy can be compromised by NA changes that emerge naturally and/or following antiviral treatment. Knowledge of which molecular changes confer drug resistance of influenza A(H7N9) viruses (group 2NA) remains sparse.

PubMed: 28934455
DOI: 10.1093/infdis/jiw625

Experimental method

X-RAY DIFFRACTION (2.4 Å)